Repozytorium

AQuaRef: machine learning accelerated quantum refinement of protein structures

Autorzy

Roman Zubatyuk

Małgorzata Biczysko

Kavindri Ranasinghe

Nigel W. Moriarty

Hatice Gokcan

Holger Kruse

Billy K. Poon

Paul D. Adams

Mark P. Waller

Adrian E. Roitberg

Olexandr Isayev

Pavel V. Afonine

Rok wydania

2025

Czasopismo

Nature Communications

Numer woluminu

16

Strony

9224/1-9224/12

DOI

10.1038/s41467-025-64313-1

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

Cryo-EM and X-ray crystallography provide crucial experimental data for obtaining atomic-detail models of biomacromolecules. Refining these models relies on library-based stereochemical data, which, in addition to being limited to known chemical entities, do not include meaningful noncovalent interactions. Quantum mechanical (QM) calculations could alleviate these issues but are too expensive for large molecules. Here we present a novel AI-enabled Quantum Refinement (AQuaRef) based on AIMNet2 machine learned interatomic potential (MLIP) mimicking QM at substantially lower computational costs. By refining 41 cryo-EM and 30 X-ray structures, we show that this approach yields atomic models with superior geometric quality compared to standard techniques, while maintaining an equal or better fit to experimental data. Notably, AQuaRef aids in determining proton positions, as illustrated in the challenging case of short hydrogen bonds in the parkinsonism-associated human protein DJ-1 and its bacterial homolog YajL.

Słowa kluczowe

Cryoelectron microscopy, Machine learning, Proteins

Licencja otwartego dostępu

CC-BY

Licencja na prawach której można swobodnie kopiować, rozprowadzać, zmieniać i remiksować objęty prawem autorskim utwór (Utwór-przedmiot prawa autorskiego) pod warunkiem podania imienia i nazwiska autora utworu pierwotnego oraz źródła pochodzenia utworu.

Pełny tekst licencji: https://creativecommons.org/licenses/by/3.0/pl/legalcode

Adres publiczny

http://dx.doi.org/10.1038/s41467-025-64313-1

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